ID   FABG_YEAST              Reviewed;         278 AA.
AC   P35731; D6VXN2;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 178.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase;
DE            EC=1.1.1.100;
DE   AltName: Full=3-ketoacyl-acyl carrier protein reductase;
GN   Name=OAR1; OrderedLocusNames=YKL055C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091862; DOI=10.1002/yea.320100008;
RA   Rasmussen S.W.;
RT   "Sequence of a 28.6 kb region of yeast chromosome XI includes the FBA1 and
RT   TOA2 genes, an open reading frame (ORF) similar to a translationally
RT   controlled tumour protein, one ORF containing motifs also found in plant
RT   storage proteins and 13 ORFs with weak or no homology to known proteins.";
RL   Yeast 10:S63-S68(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   FUNCTION.
RX   PubMed=9388293; DOI=10.1007/s002940050292;
RA   Schneider R., Brors B., Buerger F., Camrath S., Weiss H.;
RT   "Two genes of the putative mitochondrial fatty acid synthase in the genome
RT   of Saccharomyces cerevisiae.";
RL   Curr. Genet. 32:384-388(1997).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7] {ECO:0007744|PDB:4FD3}
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS).
RA   Zhang Y., Gao Y., Ning F., Niu L., Teng M.;
RT   "Crystal structure of apo-formed ymtOAR1.";
RL   Submitted (MAY-2012) to the PDB data bank.
RN   [8] {ECO:0007744|PDB:4FDA}
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-273 IN COMPLEX WITH NADP(+).
RA   Yujie Z., Yongxiang G.;
RT   "Crystal structure of Saccharomyces cerevisiae 3-oxoacyl-[acyl-carrier-
RT   protein] reductase complexed with NADPH.";
RL   Submitted (MAY-2012) to the PDB data bank.
RN   [9] {ECO:0007744|PDB:4HBG}
RP   X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) IN COMPLEX WITH NADPH.
RA   Zhang Y.J., Gao Y.X., Teng M.K.;
RT   "Crystal structure of yeast mitochondria 3-Oxoacyl-ACP Reductase OAR1.";
RL   Submitted (SEP-2012) to the PDB data bank.
CC   -!- FUNCTION: Involved in biosynthesis of fatty acids in mitochondria.
CC       {ECO:0000250, ECO:0000269|PubMed:9388293}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC         + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC         COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 1760 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X75781; CAA53417.1; -; Genomic_DNA.
DR   EMBL; Z28055; CAA81892.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09102.1; -; Genomic_DNA.
DR   PIR; S37877; S37877.
DR   RefSeq; NP_012868.1; NM_001179621.2.
DR   PDB; 4FD3; X-ray; 2.60 A; A/B/C/D/E/F=1-278.
DR   PDB; 4FDA; X-ray; 2.10 A; A=1-273.
DR   PDB; 4HBG; X-ray; 2.27 A; A=1-278.
DR   PDBsum; 4FD3; -.
DR   PDBsum; 4FDA; -.
DR   PDBsum; 4HBG; -.
DR   AlphaFoldDB; P35731; -.
DR   SMR; P35731; -.
DR   BioGRID; 34078; 420.
DR   DIP; DIP-5403N; -.
DR   IntAct; P35731; 1.
DR   STRING; 4932.YKL055C; -.
DR   MaxQB; P35731; -.
DR   PaxDb; 4932-YKL055C; -.
DR   PeptideAtlas; P35731; -.
DR   TopDownProteomics; P35731; -.
DR   EnsemblFungi; YKL055C_mRNA; YKL055C; YKL055C.
DR   GeneID; 853810; -.
DR   KEGG; sce:YKL055C; -.
DR   AGR; SGD:S000001538; -.
DR   SGD; S000001538; OAR1.
DR   VEuPathDB; FungiDB:YKL055C; -.
DR   eggNOG; KOG0725; Eukaryota.
DR   GeneTree; ENSGT00940000176504; -.
DR   HOGENOM; CLU_010194_2_10_1; -.
DR   InParanoid; P35731; -.
DR   OMA; QETETWG; -.
DR   OrthoDB; 1379432at2759; -.
DR   BioCyc; MetaCyc:YKL055C-MONOMER; -.
DR   BioCyc; YEAST:YKL055C-MONOMER; -.
DR   BRENDA; 1.1.1.100; 984.
DR   UniPathway; UPA00094; -.
DR   BioGRID-ORCS; 853810; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P35731; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P35731; Protein.
DR   GO; GO:0005739; C:mitochondrion; IMP:SGD.
DR   GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IDA:SGD.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR   GO; GO:0048038; F:quinone binding; IBA:GO_Central.
DR   GO; GO:0009060; P:aerobic respiration; IMP:SGD.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006631; P:fatty acid metabolic process; IMP:SGD.
DR   CDD; cd05233; SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR42760:SF40; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] REDUCTASE; 1.
DR   PANTHER; PTHR42760; SHORT-CHAIN DEHYDROGENASES/REDUCTASES FAMILY MEMBER; 1.
DR   Pfam; PF00106; adh_short; 2.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Mitochondrion; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..278
FT                   /note="3-oxoacyl-[acyl-carrier-protein] reductase"
FT                   /id="PRO_0000054872"
FT   ACT_SITE        182
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O93868"
FT   ACT_SITE        198
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   ACT_SITE        202
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250|UniProtKB:O93868"
FT   BINDING         13
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007744|PDB:4FDA, ECO:0007744|PDB:4HBG"
FT   BINDING         14
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007744|PDB:4FDA, ECO:0007744|PDB:4HBG"
FT   BINDING         16
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007744|PDB:4HBG"
FT   BINDING         36
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007744|PDB:4FDA, ECO:0007744|PDB:4HBG"
FT   BINDING         40
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007744|PDB:4FDA, ECO:0007744|PDB:4HBG"
FT   BINDING         44
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:L0E2Z4"
FT   BINDING         66
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007744|PDB:4FDA, ECO:0007744|PDB:4HBG"
FT   BINDING         67
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007744|PDB:4FDA, ECO:0007744|PDB:4HBG"
FT   BINDING         77
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:L0E2Z4"
FT   BINDING         122
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007744|PDB:4FDA, ECO:0007744|PDB:4HBG"
FT   BINDING         125
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007744|PDB:4FDA"
FT   BINDING         126
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007744|PDB:4FDA"
FT   BINDING         198
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007744|PDB:4FDA, ECO:0007744|PDB:4HBG"
FT   BINDING         202
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007744|PDB:4HBG"
FT   BINDING         230
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007744|PDB:4HBG"
FT   BINDING         231
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O93868"
FT   STRAND          2..11
FT                   /evidence="ECO:0007829|PDB:4FDA"
FT   HELIX           15..26
FT                   /evidence="ECO:0007829|PDB:4FDA"
FT   STRAND          30..37
FT                   /evidence="ECO:0007829|PDB:4FDA"
FT   HELIX           38..42
FT                   /evidence="ECO:0007829|PDB:4FDA"
FT   HELIX           49..52
FT                   /evidence="ECO:0007829|PDB:4FDA"
FT   STRAND          60..64
FT                   /evidence="ECO:0007829|PDB:4FDA"
FT   HELIX           67..69
FT                   /evidence="ECO:0007829|PDB:4FDA"
FT   HELIX           72..75
FT                   /evidence="ECO:0007829|PDB:4FDA"
FT   STRAND          79..84
FT                   /evidence="ECO:0007829|PDB:4FDA"
FT   STRAND          86..88
FT                   /evidence="ECO:0007829|PDB:4FDA"
FT   STRAND          91..97
FT                   /evidence="ECO:0007829|PDB:4FDA"
FT   HELIX           100..105
FT                   /evidence="ECO:0007829|PDB:4FDA"
FT   STRAND          108..119
FT                   /evidence="ECO:0007829|PDB:4FDA"
FT   HELIX           129..131
FT                   /evidence="ECO:0007829|PDB:4FDA"
FT   HELIX           134..144
FT                   /evidence="ECO:0007829|PDB:4FDA"
FT   HELIX           146..165
FT                   /evidence="ECO:0007829|PDB:4FDA"
FT   HELIX           167..171
FT                   /evidence="ECO:0007829|PDB:4FDA"
FT   STRAND          172..174
FT                   /evidence="ECO:0007829|PDB:4FD3"
FT   STRAND          177..181
FT                   /evidence="ECO:0007829|PDB:4FDA"
FT   HELIX           184..186
FT                   /evidence="ECO:0007829|PDB:4FDA"
FT   STRAND          187..189
FT                   /evidence="ECO:0007829|PDB:4FDA"
FT   HELIX           196..216
FT                   /evidence="ECO:0007829|PDB:4FDA"
FT   HELIX           217..219
FT                   /evidence="ECO:0007829|PDB:4FDA"
FT   STRAND          222..226
FT                   /evidence="ECO:0007829|PDB:4FDA"
FT   HELIX           246..251
FT                   /evidence="ECO:0007829|PDB:4HBG"
FT   HELIX           260..272
FT                   /evidence="ECO:0007829|PDB:4FDA"
SQ   SEQUENCE   278 AA;  31184 MW;  62FC3BC347D3E933 CRC64;
     MHYLPVAIVT GATRGIGKAI CQKLFQKGLS CIILGSTKES IERTAIDRGQ LQSGLSYQRQ
     CAIAIDFKKW PHWLDYESYD GIEYFKDRPP LKQKYSTLFD PCNKWSNNER RYYVNLLINC
     AGLTQESLSV RTTASQIQDI MNVNFMSPVT MTNICIKYMM KSQRRWPELS GQSARPTIVN
     ISSILHSGKM KVPGTSVYSA SKAALSRFTE VLAAEMEPRN IRCFTISPGL VKGTDMIQNL
     PVEAKEMLER TIGASGTSAP AEIAEEVWSL YSRTALET
//